1w0s

Solution structure of trimeric form of properdin by X-ray solution scattering and analytical ultracentrifugation

Method: SOLUTION SCATTERING Dmax: 251.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROPERDIN

OrganismNot specified

UniProt P27918

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 28–469 Fragment:RESIDUES 28-469 No other associated polymer SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution not provided
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 28–469 Fragment:RESIDUES 28-469 No other associated polymer SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution not provided
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 28–469 Fragment:RESIDUES 28-469 No other associated polymer SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PROP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–442; UniProt 28–469 Author chain B; PDBConstruct 1–442; UniProt 28–469 Author chain C; PDBConstruct 1–442; UniProt 28–469

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1w0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1w0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1w0s
Deposition date deposition_date2004-06-09
Structure title titleSolution structure of trimeric form of properdin by X-ray solution scattering and analytical ultracentrifugation
Keywords keywordsX-RAY SCATTERING, ANALYTICAL ULTRACENTRIFUGATION, COMPLEMENT, THROMBOSPONDIN TYPE I REPEATS, CONSTRAINED MODELLING, GLYCOPROTEIN; GLYCOPROTEIN
Experimental Method methodSOLUTION SCATTERING

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron103.00
Forward intensity I(0) i0357218000.00
Molecular weight molecular_weight145480.0 kDa
Excluded volume excluded_volume173660 ų
Envelope volume envelope_volume444560 ų
Hydration-shell volume shell_volume41760 ų
Envelope diameter envelope_diameter289.7
Shell Rg shell_rg70.91
Envelope Rg envelope_rg93.29
Shape Rg shape_rg102.50
Total Rg total_rg102.60
Total atoms total_atoms
Residues n_residues
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax251.0
Rg (real space) rg_real97.78
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real3.4160e+08
I(0) uncertainty (real space) i0_real_error6.9100e+06
Rg (reciprocal space) rg_reciprocal98.31
I(0) (reciprocal space) i0_reciprocal353100000.0000
Solution quality estimate total_estimate0.8877
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary150.6
Skewness Skewness skewness-0.003
Kurtosis Kurtosis kurtosis-1.070
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.9758
Highest regularization parameter α highest_alpha69140000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.993; Stabil: 0.921; Sysdev: 1.000; Positv: 1.000; Valcen: 0.803; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)